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2BHY

Crystal structure of Deinococcus radiodurans maltooligosyltrehalose trehalohydrolase in complex with trehalose

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0005992biological_processtrehalose biosynthetic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305
ChainResidueDetails
AASP275

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
AGLU308

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q55088
ChainResidueDetails
AARG273
AHIS399

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:15784255
ChainResidueDetails
AASP328
AGLU376

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000305
ChainResidueDetails
AASP400

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP315
AASP275

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AARG273
AASP400
AGLU308
AASP275
AHIS399

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PDB entries from 2024-11-06

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